ZN689_RAT
ID ZN689_RAT Reviewed; 500 AA.
AC Q99PJ7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Zinc finger protein 689;
DE AltName: Full=Transcription factor HIT-39;
GN Name=Znf689; Synonyms=Hit39, Zfp689;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Ishii K., Araki K., Nawa H.;
RT "Cloning and characterization of a novel transcription factor HIT-39 in the
RT brain.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF277902; AAG53888.1; -; mRNA.
DR RefSeq; NP_775452.1; NM_173330.1.
DR AlphaFoldDB; Q99PJ7; -.
DR SMR; Q99PJ7; -.
DR STRING; 10116.ENSRNOP00000024969; -.
DR PaxDb; Q99PJ7; -.
DR Ensembl; ENSRNOT00000024969; ENSRNOP00000024969; ENSRNOG00000066277.
DR GeneID; 286996; -.
DR KEGG; rno:286996; -.
DR UCSC; RGD:628696; rat.
DR CTD; 71131; -.
DR RGD; 628696; Zfp689.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162326; -.
DR HOGENOM; CLU_002678_13_1_1; -.
DR InParanoid; Q99PJ7; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q99PJ7; -.
DR TreeFam; TF336948; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR PRO; PR:Q99PJ7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018877; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q99PJ7; baseline and differential.
DR Genevisible; Q99PJ7; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..500
FT /note="Zinc finger protein 689"
FT /id="PRO_0000234010"
FT DOMAIN 29..100
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 149..171
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 177..199
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 205..227
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..255
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..482
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96CS4"
SQ SEQUENCE 500 AA; 57282 MW; 7F4D21648E6DE026 CRC64;
MAPPSAPLLE QAPGEVGPTR RRGRRPRALK FADVAVYFSS EEWGRLRPAQ RTLYRDVMRE
TYGLLGALGC AGPKPALITW LERNTDDWEP AALDPQEYRR WVTFQRKTRT RQKNEEKEVF
PPKDVPRKGK RGRKPSKPRL IARQTSGGPI CPDCGCTFPD LPALESHKCA QNLKKPYPCP
DCGRRFSYPS LLVSHRRAHS GECPYVCDQC GKRFSQRKNL SQHQVIHTGE KPYHCPDCGR
CFRRSRSLAN HRTTHTGEKP HQCPSCGRRF AYPSLLAIHQ RTHTGEKPYT CLECSRRFRQ
RTALVIHQRI HTGEKPYPCP DCERRFSSSS RLVSHRRVHS GERPYACEHC EARFSQRSTL
LQHQLLHTGE KPYPCPDCGR AFRRSGSLAI HRSTHTEEKL HACDDCGRRF AYPSLLASHR
RVHSGERPYA CDLCSKRFAQ WSHLAQHQLL HTGEKPFPCL ECGRCFRQRW SLAVHKCCPN
THNGSPRPLI GGPNQRSSAL
